Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
SmLMWPTP, a teleost low molecular weight protein tyrosine phosphatase, inhibits the immune response of peripheral blood leukocytes in a manner that depends on the conserved P-loop | |
Zhang, Jian1,2; Chen, Ling1,2; Sun, Li1; Sun, L | |
2013-06-01 | |
发表期刊 | DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY |
ISSN | 0145-305X |
卷号 | 40期号:2页码:103-111 |
文章类型 | Article |
摘要 | Protein tyrosine phosphatases (PTPs) are a family of enzymes that play a key role in cellular signal transduction. Low molecular weight PTPs (LMWPTPs) are a subfamily of PTPs that are characterized by the presence of a conserved phosphate-binding loop (P-loop) with the signature sequence of (V/I)CXGNXCRS. To date, very little study on teleost LMWPTPs has been documented, and, as a result, the function of LMWPTPs in fish is essentially unknown. In this study, we identified a LMWPTP from turbot (Scophthalmus maximus) and examined its biological activity and functionality. The turbot LMWPTP (SmLMWPTP) is composed of 158 residues and possesses a typical P-loop sequence in the form of (12)VCLGNICRS(20). Purified recombinant SmLMWPTP (rSmLMWPTP) exhibited apparent phosphatase activity, which was optimal at pH 5 and 50 degrees C. The activity of SmLMWPTP was abolished when C13 and, in particular, R19 of the P-loop were mutated. SmLMWPTP expression was detected in a wide range of tissues and upregulated by bacterial and viral infection. Subcellular localization analysis showed that SmLMWPTP was secreted by peripheral blood leukocytes (PBL) into the extracellular milieu. When PBL were treated with rSmLMWPTP, the cells exhibited significant reductions in (i) proliferative and respiratory burst activity, (ii) expression levels of multiple immune relevant genes, and (iii) phagocytic activity. In contrast, the mutant SmLMWPTP bearing R19 mutation had no effect on PBL activity. Taken together, these results indicate that SmLMWPTP is a secreted PTP that exerts a negative regulatory effect on the innate immune response of PBL in a manner that depends on the structural integrity of the P-loop. (C) 2013 Elsevier Ltd. All rights reserved.; Protein tyrosine phosphatases (PTPs) are a family of enzymes that play a key role in cellular signal transduction. Low molecular weight PTPs (LMWPTPs) are a subfamily of PTPs that are characterized by the presence of a conserved phosphate-binding loop (P-loop) with the signature sequence of (V/I)CXGNXCRS. To date, very little study on teleost LMWPTPs has been documented, and, as a result, the function of LMWPTPs in fish is essentially unknown. In this study, we identified a LMWPTP from turbot (Scophthalmus maximus) and examined its biological activity and functionality. The turbot LMWPTP (SmLMWPTP) is composed of 158 residues and possesses a typical P-loop sequence in the form of (12)VCLGNICRS(20). Purified recombinant SmLMWPTP (rSmLMWPTP) exhibited apparent phosphatase activity, which was optimal at pH 5 and 50 degrees C. The activity of SmLMWPTP was abolished when C13 and, in particular, R19 of the P-loop were mutated. SmLMWPTP expression was detected in a wide range of tissues and upregulated by bacterial and viral infection. Subcellular localization analysis showed that SmLMWPTP was secreted by peripheral blood leukocytes (PBL) into the extracellular milieu. When PBL were treated with rSmLMWPTP, the cells exhibited significant reductions in (i) proliferative and respiratory burst activity, (ii) expression levels of multiple immune relevant genes, and (iii) phagocytic activity. In contrast, the mutant SmLMWPTP bearing R19 mutation had no effect on PBL activity. Taken together, these results indicate that SmLMWPTP is a secreted PTP that exerts a negative regulatory effect on the innate immune response of PBL in a manner that depends on the structural integrity of the P-loop. (C) 2013 Elsevier Ltd. All rights reserved. |
关键词 | Protein Tyrosine Phosphatase Scophthalmus Maximus Immune Regulation Phagocytosis |
学科领域 | Immunology ; Zoology |
DOI | 10.1016/j.dci.2013.03.001 |
URL | 查看原文 |
收录类别 | SCI |
语种 | 英语 |
WOS研究方向 | Immunology ; Zoology |
WOS类目 | Immunology ; Zoology |
WOS记录号 | WOS:000320491100003 |
WOS关键词 | PHOSPHOTYROSINE PHOSPHATASE ; CRYSTAL-STRUCTURE ; SCOPHTHALMUS-MAXIMUS ; LMW-PTP ; EXPRESSION ; GROWTH ; STIMULATION ; DEPHOSPHORYLATION ; PHOSPHORYLATION ; INACTIVATION |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.qdio.ac.cn/handle/337002/16521 |
专题 | 实验海洋生物学重点实验室 |
通讯作者 | Sun, L |
作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China |
第一作者单位 | 实验海洋生物学重点实验室 |
推荐引用方式 GB/T 7714 | Zhang, Jian,Chen, Ling,Sun, Li,et al. SmLMWPTP, a teleost low molecular weight protein tyrosine phosphatase, inhibits the immune response of peripheral blood leukocytes in a manner that depends on the conserved P-loop[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2013,40(2):103-111. |
APA | Zhang, Jian,Chen, Ling,Sun, Li,&Sun, L.(2013).SmLMWPTP, a teleost low molecular weight protein tyrosine phosphatase, inhibits the immune response of peripheral blood leukocytes in a manner that depends on the conserved P-loop.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,40(2),103-111. |
MLA | Zhang, Jian,et al."SmLMWPTP, a teleost low molecular weight protein tyrosine phosphatase, inhibits the immune response of peripheral blood leukocytes in a manner that depends on the conserved P-loop".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 40.2(2013):103-111. |
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a teleost low molecu(1911KB) | 限制开放 | CC BY-NC-SA | 浏览 |
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